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Fichtenbaum, C.J.1
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C. J. Fichtenbaum and W. C. Powderly, Clin. Infect. Dis. 26, 556 (1998); J. H. Rex, T. J. Walsh, E. J. Anaissie, Adv. Int. Med. 43, 321 (1998).
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Rex, J.H.1
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0001490507
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M. Darmon and M. Blumenberg, Eds. Academic Press, San Diego, CA, chap. 4
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U. Reichert, S. Michel, R. Schmidt, in Molecular Biology of the Skin: The Keratinocyte, M. Darmon and M. Blumenberg, Eds. (Academic Press, San Diego, CA, 1993), chap. 4, p. 107.
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Reichert, U.1
Michel, S.2
Schmidt, R.3
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9
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0344148903
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note
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2-terminus of the mature protein through the proline- and glutamine-rich-repeats [amino acids 40 to 197 encoded by HWP1 cDNA (2)], was purified from culture media of Pichia pastoris by anion-exchange chromatography (Mono Q, Bio-Rad), with a salt gradient (0 to 1 M NaCl) in column buffer [50 mM tris-HCl (pH 8), 2 mM mercaptoethanol, 1 mM EDTA].
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12
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0030983922
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M. T. Kaartinen, A. Pirhonen, A. Linnala-Kankkunen, P. H. Maenpaa, ibid. 272, 22736 (1997).
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J. Biol. Chem.
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Kaartinen, M.T.1
Pirhonen, A.2
Linnala-Kankkunen, A.3
Maenpaa, P.H.4
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14
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0015151656
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L. Lorand, O. M. Lockridge, L. K. Campbell, R. Myhrman, J. Bruner-Lorand, Anal. Biochem. 44, 221 (1971); P. T. Velasco, F. Karush, L. Lorand, Biochem. Biophys. Res. Commun. 152, 505 (1988); L. Lorand, L. K. Campbell-Wilkes, L. Cooperstein, Anal. Biochem. 50, 623 (1972).
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Lorand, L.1
Lockridge, O.M.2
Campbell, L.K.3
Myhrman, R.4
Bruner-Lorand, J.5
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L. Lorand, O. M. Lockridge, L. K. Campbell, R. Myhrman, J. Bruner-Lorand, Anal. Biochem. 44, 221 (1971); P. T. Velasco, F. Karush, L. Lorand, Biochem. Biophys. Res. Commun. 152, 505 (1988); L. Lorand, L. K. Campbell-Wilkes, L. Cooperstein, Anal. Biochem. 50, 623 (1972).
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Velasco, P.T.1
Karush, F.2
Lorand, L.3
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16
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0015463837
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L. Lorand, O. M. Lockridge, L. K. Campbell, R. Myhrman, J. Bruner-Lorand, Anal. Biochem. 44, 221 (1971); P. T. Velasco, F. Karush, L. Lorand, Biochem. Biophys. Res. Commun. 152, 505 (1988); L. Lorand, L. K. Campbell-Wilkes, L. Cooperstein, Anal. Biochem. 50, 623 (1972).
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Lorand, L.1
Campbell-Wilkes, L.K.2
Cooperstein, L.3
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18
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0027192868
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+ homozygous hwp1/hwp1 strain, CAH7-1A1, with Hind III-digested pGBHWP1 and p24enura (20) digested with Xba I-Xho I, resulting in an enolase gene disrupted with URA3. Generation times of CAH7, CAH7-1A, and CAHR3 were 2.52, 2.57, and 2.57 hours, respectively, whereas that of SC5314 was 2.00 hours in YNB at 27°C.
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(1993)
Genetics
, vol.134
, pp. 717
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Fonzi, W.A.1
Irwin, M.Y.2
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19
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0345011399
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note
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Hwp1 was assessed with monospecific antiserum to rHwp1 in indirect immunofluorescence assays (2).
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20
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0345442497
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note
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2, 1 mM EDTA, 1 mM dithiothreitol (DTT)], at a germ tube/BEC ratio of 100:1 and incubated for 1 hour at 37°C, followed by reaction termination with 100 mM ECTA (75 μl). For overall adhesion, radioactivity of BEC fractions was determined by scintillation counting after centrifugation on 50% Percoll gradients (27), and the number of germ tubes per BEC was determined with the specific activity of each strain. For stabilized adhesion assays, reaction mixtures were heated to 100°C for 2 min in phosphate-buffered saline (PBS) containing 1% SDS before loading on Percoll gradients. Monodansylcadaverine (5 mM) or iodoacetamide (10 mM) was used to inhibit TGase during the 1-hour incubation at 37°C. Subtracted background counts, determined from gradients lacking BECs, were less than 6% of counts for BEC-associated counts. Visual counting confirmed results with radiolabeled cells.
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22
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0345442496
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note
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5 BECs in 300 μl of reaction buffer 3 under stabilized adhesion assay conditions (17). BECs were washed in 500 μl of PBS, suspended in 50 μl of sample buffer (23), boiled for 5 min, vortexed, and centrifuged. Supernatants containing unbound proteins were discarded and BECs were suspended in PBS (50 μl) and transferred to vials with scintillation fluid to determine BEC-associated dpm.
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28
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0344148895
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note
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2,1 mM DTT, 1 mM EDTA] for 30 min at 37°C (total volume, 25 μl). Radioactivity bound to acceptor proteins was assessed by scintillation counting after trichloroacetic acid precipitation. Background counts from reactions without acceptor proteins were subtracted from total counts (13).
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29
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0345011398
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note
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Reactions (25) were incubated for 4 hours and quenched with cold putrescine (100 mM) for 1 hour before boiling in Laemmli sample buffer (23) for 5 min.
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31
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0004136246
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Cold Spring Harbor Laboratory, Cold Spring Harbor, NY
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J. Sambrook, E. F. Fritsch, T. Maniatis, Molecular Cloning: A Laboratory Manual (Cold Spring Harbor Laboratory, Cold Spring Harbor, NY, 1989), pp. 18.17-18.18.
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(1989)
Molecular Cloning: A Laboratory Manual
, pp. 1817-1818
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Sambrook, J.1
Fritsch, E.F.2
Maniatis, T.3
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32
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0345442495
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note
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Organisms were grown for 18 hours in phytonepeptone broth supplemented with 0.1% glucose at 25°C with shaking at 100 rpm.
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33
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0345011394
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note
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Animal studies were conducted in accordance with the NIH guidelines for the care and use of laboratory animals. We thank A. Jackson for assistance with preparation of TGase2, B. Taylor for assistance with the animal experiments, and C. M. Allen for histological assessments of infected mouse tissues. Support for this research was provided from grant 1 RO1 DE11375-05A2 from the National Institute of Dental and Craniofacial Research (P.S.) and AI32556 from the National Institute for Allergy and Infectious Diseases (P.L.F.).
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